Magnesium in PDB 1yns: Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog

The structure of Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog, PDB code: 1yns was solved by H.Wang, H.Pang, M.Bartlam, Z.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.017, 57.546, 87.318, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 23.4

The binding sites of Magnesium atom in the Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog (pdb code 1yns). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog, PDB code: 1yns:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1258 b:17.2 occ:1.00 O A:HOH1831 2.0 19.4 1.0 OD1 A:ASP212 2.0 15.0 1.0 O A:HOH1835 2.1 18.4 1.0 OD2 A:ASP16 2.1 16.8 1.0 O A:GLU18 2.1 15.4 1.0 O A:HOH1834 2.1 17.3 1.0 CG A:ASP16 3.0 18.9 1.0 CG A:ASP212 3.1 18.5 1.0 OD1 A:ASP16 3.3 17.9 1.0 C A:GLU18 3.3 16.3 1.0 OD2 A:ASP212 3.4 17.9 1.0 O A:HOH1463 4.0 48.7 1.0 CA A:GLU18 4.1 16.4 1.0 OG1 A:THR20 4.1 15.0 1.0 CB A:GLU18 4.3 15.6 1.0 N A:GLU18 4.3 14.0 1.0 N A:GLY19 4.3 15.5 1.0 CG2 A:VAL213 4.3 23.2 1.0 O3 A:HPO1261 4.4 39.3 1.0 CB A:ASP16 4.4 18.2 1.0 CB A:ASP212 4.4 18.8 1.0 N A:ASP212 4.4 17.9 1.0 OG1 A:THR211 4.4 18.3 1.0 CA A:GLY19 4.5 16.6 1.0 CG A:GLU18 4.7 19.6 1.0 O A:HOH1471 4.7 50.5 1.0 O A:HOH1366 4.8 48.0 1.0 C A:GLY19 4.8 19.0 1.0 N A:THR20 4.8 17.4 1.0 N A:VAL213 4.8 18.7 1.0 OE2 A:GLU216 4.8 20.7 1.0 OE1 A:GLU216 4.8 19.2 1.0 C A:ILE17 4.8 15.0 1.0 CA A:ASP212 4.9 17.3 1.0 NZ A:LYS187 4.9 23.7 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1259 b:18.2 occ:1.00 OD1 A:ASP198 2.0 14.7 1.0 O A:HOH1838 2.1 22.6 1.0 O A:HOH1839 2.1 20.3 1.0 O A:HOH1832 2.1 19.2 1.0 O A:HOH1836 2.2 14.3 1.0 O A:HOH1837 2.3 15.9 1.0 CG A:ASP198 3.0 16.4 1.0 OD2 A:ASP198 3.4 15.5 1.0 O A:HOH1532 4.1 23.6 1.0 O A:HOH1542 4.2 22.6 1.0 O A:ARG194 4.2 14.8 1.0 CB A:ASP198 4.4 16.9 1.0 CA A:ASP198 4.6 17.0 1.0 N A:ASP198 4.6 16.5 1.0 O A:CYS202 4.9 15.6 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human Enolase-Phosphatase E1 and Its Complex with A Substrate Analog within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1260 b:25.6 occ:1.00 O A:HOH1843 1.9 23.0 1.0 O A:HOH1840 2.0 36.4 1.0 O A:HOH1833 2.0 21.5 1.0 O A:HOH1842 2.1 23.7 1.0 O A:HOH1844 2.3 33.2 1.0 O A:HOH1841 2.3 27.8 1.0 O A:HOH1723 3.9 72.4 1.0 OE2 A:GLU9 4.1 25.4 1.0 OD1 A:ASP224 4.3 22.4 1.0 OE1 A:GLU9 4.3 26.4 1.0 CB A:ASN205 4.3 21.6 1.0 O A:HOH1621 4.4 25.9 1.0 OD2 A:ASP224 4.5 21.8 1.0 CD A:GLU9 4.6 23.0 1.0 CG A:ASP224 4.8 22.7 1.0 CG A:ASN205 4.9 22.1 1.0

H.Wang, H.Pang, M.Bartlam, Z.Rao. Crystal Structure of Human E1 Enzyme and Its Complex with A Substrate Analog Reveals the Mechanism of Its Phosphatase/Enolase J.Mol.Biol. V. 348 917 2005.
ISSN: ISSN 0022-2836
PubMed: 15843022
DOI: 10.1016/J.JMB.2005.01.072